The overall goal of this work is to develop and evaluate stationary phase in conjunction with mobile phase control for the high speed separation of proteins and peptides. Work to-date has concentrated on achieving reproducible and highly efficient reversed phase materials for PTH-amino acids, peptides and small molecular weight proteins. Other studies have dealt with a polar diol bonded phase for size exclusion chromatography of proteins. By variation of the ionic strength and by addition of ethylene glycol, the interaction of various proteins with the stationary phase could be elucidated. Work is continuing on devising polar bonded phases and dynamically coated hydrophilic phases for separation of peptides and proteins. Finally, these columns are currently being applied in several areas including the separation of high molecular weight proteoglycans from human cartilage. Such species are known to undergo changes in osteoarthritis and aging.